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P32019

- I5P2_HUMAN

UniProt

P32019 - I5P2_HUMAN

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Protein

Type II inositol 1,4,5-trisphosphate 5-phosphatase

Gene

INPP5B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Hydrolyzes phosphatidylinositol 4,5-bisphosphate (PtIns(4,5)P2) and the signaling molecule phosphatidylinositol 1,4,5-trisphosphate (PtIns(1,4,5)P3), and thereby modulates cellular signaling events.1 Publication

Catalytic activityi

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi355 – 3551Magnesium1 Publication
Metal bindingi383 – 3831Magnesium1 Publication
Binding sitei383 – 3831Substrate

GO - Molecular functioni

  1. inositol-1,4,5-trisphosphate 5-phosphatase activity Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW
  3. phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity Source: UniProtKB

GO - Biological processi

  1. inositol phosphate metabolic process Source: Reactome
  2. in utero embryonic development Source: Ensembl
  3. phosphatidylinositol dephosphorylation Source: UniProtKB
  4. regulation of protein processing Source: Ensembl
  5. regulation of small GTPase mediated signal transduction Source: Reactome
  6. small GTPase mediated signal transduction Source: Reactome
  7. small molecule metabolic process Source: Reactome
  8. spermatogenesis Source: Ensembl
  9. sperm motility Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS05898-MONOMER.
BRENDAi3.1.3.36. 2681.
ReactomeiREACT_11051. Rho GTPase cycle.
REACT_150312. Synthesis of IP3 and IP4 in the cytosol.
REACT_150352. Synthesis of IP2, IP, and Ins in the cytosol.
SABIO-RKP32019.

Names & Taxonomyi

Protein namesi
Recommended name:
Type II inositol 1,4,5-trisphosphate 5-phosphatase (EC:3.1.3.36)
Alternative name(s):
75 kDa inositol polyphosphate-5-phosphatase
Phosphoinositide 5-phosphatase
Short name:
5PTase
Gene namesi
Name:INPP5B
Synonyms:OCRL2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:6077. INPP5B.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytoplasmic vesicle Source: UniProtKB-KW
  3. cytosol Source: UniProtKB
  4. endosome Source: UniProtKB-KW
  5. Golgi apparatus Source: UniProtKB-KW
  6. integral component of membrane Source: Ensembl
  7. membrane Source: UniProtKB
  8. microtubule cytoskeleton Source: HPA
  9. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Endosome, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi990 – 9901C → S: Loss of prenylation and membrane localization. 1 Publication

Organism-specific databases

PharmGKBiPA29885.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 990990Type II inositol 1,4,5-trisphosphate 5-phosphatasePRO_0000015640Add
BLAST
Propeptidei991 – 9933Removed in mature formSequence AnalysisPRO_0000422293

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei990 – 9901Cysteine methyl esterSequence Analysis
Lipidationi990 – 9901S-farnesyl cysteineSequence Analysis

Post-translational modificationi

Isoprenylation at Cys-990 may be required for localization at the membrane.1 Publication
May be proteolytically cleaved after Lys-320 as inferred from N-terminal protein sequence of the 75 kda form.1 Publication

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

MaxQBiP32019.
PaxDbiP32019.
PRIDEiP32019.

PTM databases

PhosphoSiteiP32019.

Expressioni

Tissue specificityi

Platelets.

Gene expression databases

BgeeiP32019.
CleanExiHS_INPP5B.
ExpressionAtlasiP32019. baseline and differential.
GenevestigatoriP32019.

Organism-specific databases

HPAiHPA028803.

Interactioni

Subunit structurei

Interacts with APPL1, FAM109A and FAM109B. Interacts with several Rab GTPases, at least RAB1A, RAB2A, RAB5A, RAB6A, RAB8A, RAB9A and RAB33B; these interactions may play a dual role in targeting INPP5B to the specific membranes and stimulating the phosphatase activity.4 Publications

Protein-protein interaction databases

BioGridi109845. 2 interactions.
STRINGi9606.ENSP00000362115.

Structurei

Secondary structure

1
993
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi340 – 35314Combined sources
Helixi364 – 3674Combined sources
Beta strandi368 – 3703Combined sources
Beta strandi375 – 3828Combined sources
Helixi388 – 3914Combined sources
Helixi397 – 40913Combined sources
Beta strandi416 – 4249Combined sources
Beta strandi427 – 4348Combined sources
Helixi435 – 4406Combined sources
Beta strandi441 – 45010Combined sources
Helixi453 – 4553Combined sources
Beta strandi460 – 46910Combined sources
Beta strandi472 – 4809Combined sources
Helixi485 – 4873Combined sources
Helixi488 – 50114Combined sources
Beta strandi509 – 5113Combined sources
Beta strandi518 – 52710Combined sources
Helixi537 – 5459Combined sources
Helixi549 – 5535Combined sources
Helixi557 – 5637Combined sources
Beta strandi588 – 5914Combined sources
Beta strandi604 – 62017Combined sources
Beta strandi626 – 6294Combined sources
Beta strandi632 – 64312Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MTCX-ray2.40A339-643[»]
3N9VX-ray2.65A/B342-646[»]
4CMLX-ray2.30A339-643[»]
ProteinModelPortaliP32019.
SMRiP32019. Positions 1-155, 339-643, 656-989.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32019.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 148127PHAdd
BLAST
Domaini821 – 993173Rho-GAPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni342 – 6683275-phosphataseBy similarityAdd
BLAST
Regioni459 – 4602Substrate binding
Regioni582 – 5832Substrate binding
Regioni596 – 5983Substrate binding
Regioni669 – 782114ASHBy similarityAdd
BLAST

Domaini

The ASH (ASPM-SPD2-Hydin) and RhoGAP (Rho GTPase activating) domains form a single folding module. The ASH domain has an immunoglobulin-like fold, the Rho-GAP domain lacks the catalytic arginine and is catalytically inactive. The ASH-RhoGAP module regulates the majority of the protein-protein interactions currently described. The ASH domain mediates association with membrane-targeting Rab GTPases. The Rho-GAP domain interacts with the endocytic adapter APPL1, which is then displaced by FAM109A and FAM109B as endosomes mature, all three interactions relie on F&H motifs, an approximately 12-13 amino-acid sequence centered around Phe and His residues essential for binding (By similarity).By similarity

Sequence similaritiesi

Contains 1 PH domain.Curated
Contains 1 Rho-GAP domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5411.
GeneTreeiENSGT00760000119075.
HOVERGENiHBG000070.
InParanoidiP32019.
KOiK01099.
OMAiPMEIPKE.
OrthoDBiEOG7J4465.
PhylomeDBiP32019.
TreeFamiTF317034.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
3.60.10.10. 1 hit.
InterProiIPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamiPF03372. Exo_endo_phos. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTiSM00128. IPPc. 1 hit.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 2 hits.
SSF56219. SSF56219. 1 hit.
PROSITEiPS50238. RHOGAP. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P32019-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDQSVAIQET LAEGEYCVIA VQGVLCEGDS RQSRLLGLVR YRLEHGGQEH
60 70 80 90 100
ALFLYTHRRM AITGDDVSLD QIVPVSRDFT LEEVSPDGEL YILGSDVTVQ
110 120 130 140 150
LDTAELSLVF QLPFGSQTRM FLHEVARACP GFDSATRDPE FLWLSRYRCA
160 170 180 190 200
ELELEMPTPR GCNSALVTWP GYATIGGGRY PSRKKRWGLE EARPQGAGSV
210 220 230 240 250
LFWGGAMEKT GFRLMERAHG GGFVWGRSAR DGRRDEELEE AGREMSAAAG
260 270 280 290 300
SRERNTAGGS NFDGLRPNGK GVPMDQSSRG QDKPESLQPR QNKSKSEITD
310 320 330 340 350
MVRSSTITVS DKAHILSMQK FGLRDTIVKS HLLQKEEDYT YIQNFRFFAG
360 370 380 390 400
TYNVNGQSPK ECLRLWLSNG IQAPDVYCVG FQELDLSKEA FFFHDTPKEE
410 420 430 440 450
EWFKAVSEGL HPDAKYAKVK LIRLVGIMLL LYVKQEHAAY ISEVEAETVG
460 470 480 490 500
TGIMGRMGNK GGVAIRFQFH NTSICVVNSH LAAHIEEYER RNQDYKDICS
510 520 530 540 550
RMQFCQPDPS LPPLTISNHD VILWLGDLNY RIEELDVEKV KKLIEEKDFQ
560 570 580 590 600
MLYAYDQLKI QVAAKTVFEG FTEGELTFQP TYKYDTGSDD WDTSEKCRAP
610 620 630 640 650
AWCDRILWKG KNITQLSYQS HMALKTSDHK PVSSVFDIGV RVVNDELYRK
660 670 680 690 700
TLEEIVRSLD KMENANIPSV SLSKREFCFQ NVKYMQLKVE SFTIHNGQVP
710 720 730 740 750
CHFEFINKPD EESYCKQWLN ANPSRGFLLP DSDVEIDLEL FVNKMTATKL
760 770 780 790 800
NSGEDKIEDI LVLHLDRGKD YFLSVSGNYL PSCFGSPIHT LCYMREPILD
810 820 830 840 850
LPLETISELT LMPVWTGDDG SQLDSPMEIP KELWMMVDYL YRNAVQQEDL
860 870 880 890 900
FQQPGLRSEF EHIRDCLDTG MIDNLSASNH SVAEALLLFL ESLPEPVICY
910 920 930 940 950
STYHNCLECS GNYTASKQVI STLPIFHKNV FHYLMAFLRE LLKNSAKNHL
960 970 980 990
DENILASIFG SLLLRNPAGH QKLDMTEKKK AQEFIHQFLC NPL

Note: No experimental confirmation available.

Length:993
Mass (Da):112,852
Last modified:December 15, 2009 - v4
Checksum:iABD3581CC6CD29D6
GO
Isoform 2 (identifier: P32019-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     178-257: Missing.

Show »
Length:913
Mass (Da):103,987
Checksum:i4882C26F6E4DC9C6
GO
Isoform 3 (identifier: P32019-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-244: Missing.

Show »
Length:749
Mass (Da):85,620
Checksum:i50921FAACF7E1E39
GO
Isoform 4 (identifier: P32019-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     810-828: TLMPVWTGDDGSQLDSPME → LAYLAAYCFETQLVTKSLI
     829-993: Missing.

Note: No experimental confirmation available.

Show »
Length:828
Mass (Da):93,924
Checksum:i9CD5C12DCF509A50
GO

Sequence cautioni

The sequence AAA79207.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti587 – 60620GSDDW…WCDRI → RALTTGIPVRSAVLLPGVIG F AA sequence (PubMed:1718960)CuratedAdd
BLAST
Sequence conflicti911 – 9111G → P AA sequence (PubMed:1718960)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti46 – 461G → S.
Corresponds to variant rs56993041 [ dbSNP | Ensembl ].
VAR_061270
Natural varianti745 – 7451M → T.3 Publications
Corresponds to variant rs11488569 [ dbSNP | Ensembl ].
VAR_028002

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 244244Missing in isoform 3. CuratedVSP_012821Add
BLAST
Alternative sequencei178 – 25780Missing in isoform 2. 1 PublicationVSP_012820Add
BLAST
Alternative sequencei810 – 82819TLMPV…DSPME → LAYLAAYCFETQLVTKSLI in isoform 4. 1 PublicationVSP_013902Add
BLAST
Alternative sequencei829 – 993165Missing in isoform 4. 1 PublicationVSP_013903Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74161 mRNA. Translation: AAA79207.1. Different initiation.
AL603790, AL929472 Genomic DNA. Translation: CAH69926.1.
AL603790, AL929472 Genomic DNA. Translation: CAH69928.1.
AL603790, AL929472 Genomic DNA. Translation: CAH69929.1.
AL929472, AL603790 Genomic DNA. Translation: CAH70076.1.
AL929472, AL603790 Genomic DNA. Translation: CAH70079.1.
AL929472, AL603790 Genomic DNA. Translation: CAH70080.1.
BX296560 Genomic DNA. No translation available.
BC042529 mRNA. Translation: AAH42529.2.
BC058932 mRNA. Translation: AAH58932.1.
AL833055 mRNA. Translation: CAH56301.1.
CCDSiCCDS41306.1. [P32019-2]
CCDS72760.1. [P32019-3]
RefSeqiNP_001284363.1. NM_001297434.1. [P32019-3]
NP_005531.2. NM_005540.2. [P32019-2]
UniGeneiHs.449942.

Genome annotation databases

EnsembliENST00000373023; ENSP00000362114; ENSG00000204084. [P32019-1]
ENST00000373024; ENSP00000362115; ENSG00000204084. [P32019-2]
ENST00000373026; ENSP00000362117; ENSG00000204084. [P32019-1]
ENST00000373027; ENSP00000362118; ENSG00000204084. [P32019-3]
GeneIDi3633.
KEGGihsa:3633.
UCSCiuc001ccf.1. human. [P32019-1]
uc001ccg.1. human. [P32019-2]

Polymorphism databases

DMDMi281185510.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74161 mRNA. Translation: AAA79207.1 . Different initiation.
AL603790 , AL929472 Genomic DNA. Translation: CAH69926.1 .
AL603790 , AL929472 Genomic DNA. Translation: CAH69928.1 .
AL603790 , AL929472 Genomic DNA. Translation: CAH69929.1 .
AL929472 , AL603790 Genomic DNA. Translation: CAH70076.1 .
AL929472 , AL603790 Genomic DNA. Translation: CAH70079.1 .
AL929472 , AL603790 Genomic DNA. Translation: CAH70080.1 .
BX296560 Genomic DNA. No translation available.
BC042529 mRNA. Translation: AAH42529.2 .
BC058932 mRNA. Translation: AAH58932.1 .
AL833055 mRNA. Translation: CAH56301.1 .
CCDSi CCDS41306.1. [P32019-2 ]
CCDS72760.1. [P32019-3 ]
RefSeqi NP_001284363.1. NM_001297434.1. [P32019-3 ]
NP_005531.2. NM_005540.2. [P32019-2 ]
UniGenei Hs.449942.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3MTC X-ray 2.40 A 339-643 [» ]
3N9V X-ray 2.65 A/B 342-646 [» ]
4CML X-ray 2.30 A 339-643 [» ]
ProteinModelPortali P32019.
SMRi P32019. Positions 1-155, 339-643, 656-989.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109845. 2 interactions.
STRINGi 9606.ENSP00000362115.

PTM databases

PhosphoSitei P32019.

Polymorphism databases

DMDMi 281185510.

Proteomic databases

MaxQBi P32019.
PaxDbi P32019.
PRIDEi P32019.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000373023 ; ENSP00000362114 ; ENSG00000204084 . [P32019-1 ]
ENST00000373024 ; ENSP00000362115 ; ENSG00000204084 . [P32019-2 ]
ENST00000373026 ; ENSP00000362117 ; ENSG00000204084 . [P32019-1 ]
ENST00000373027 ; ENSP00000362118 ; ENSG00000204084 . [P32019-3 ]
GeneIDi 3633.
KEGGi hsa:3633.
UCSCi uc001ccf.1. human. [P32019-1 ]
uc001ccg.1. human. [P32019-2 ]

Organism-specific databases

CTDi 3633.
GeneCardsi GC01M038326.
HGNCi HGNC:6077. INPP5B.
HPAi HPA028803.
MIMi 147264. gene.
neXtProti NX_P32019.
PharmGKBi PA29885.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5411.
GeneTreei ENSGT00760000119075.
HOVERGENi HBG000070.
InParanoidi P32019.
KOi K01099.
OMAi PMEIPKE.
OrthoDBi EOG7J4465.
PhylomeDBi P32019.
TreeFami TF317034.

Enzyme and pathway databases

BioCyci MetaCyc:HS05898-MONOMER.
BRENDAi 3.1.3.36. 2681.
Reactomei REACT_11051. Rho GTPase cycle.
REACT_150312. Synthesis of IP3 and IP4 in the cytosol.
REACT_150352. Synthesis of IP2, IP, and Ins in the cytosol.
SABIO-RK P32019.

Miscellaneous databases

ChiTaRSi INPP5B. human.
EvolutionaryTracei P32019.
GeneWikii INPP5B.
GenomeRNAii 3633.
NextBioi 14219.
PROi P32019.
SOURCEi Search...

Gene expression databases

Bgeei P32019.
CleanExi HS_INPP5B.
ExpressionAtlasi P32019. baseline and differential.
Genevestigatori P32019.

Family and domain databases

Gene3Di 1.10.555.10. 1 hit.
3.60.10.10. 1 hit.
InterProi IPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view ]
Pfami PF03372. Exo_endo_phos. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view ]
SMARTi SM00128. IPPc. 1 hit.
SM00324. RhoGAP. 1 hit.
[Graphical view ]
SUPFAMi SSF48350. SSF48350. 2 hits.
SSF56219. SSF56219. 1 hit.
PROSITEi PS50238. RHOGAP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Properties of type II inositol polyphosphate 5-phosphatase."
    Jefferson A.B., Majerus P.W.
    J. Biol. Chem. 270:9370-9377(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ISOPRENYLATION AT CYS-990, MUTAGENESIS OF CYS-990, VARIANT THR-745.
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1; 2 AND 3).
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), VARIANT THR-745.
    Tissue: Lymph.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-178.
    Tissue: Stomach.
  5. "Cloning and expression of human 75-kDa inositol polyphosphate-5-phosphatase."
    Ross T.S., Jefferson A.B., Mitchell C.A., Majerus P.W.
    J. Biol. Chem. 266:20283-20289(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 284-954, PROTEIN SEQUENCE OF 321-339, VARIANT THR-745.
    Tissue: Placenta.
  6. "Targeting of the type II inositol polyphosphate 5-phosphatase INPP5B to the early secretory pathway."
    Williams C., Choudhury R., McKenzie E., Lowe M.
    J. Cell Sci. 120:3941-3951(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH RAB GTPASES.
  7. "Two closely related endocytic proteins that share a common OCRL-binding motif with APPL1."
    Swan L.E., Tomasini L., Pirruccello M., Lunardi J., De Camilli P.
    Proc. Natl. Acad. Sci. U.S.A. 107:3511-3516(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FAM109A.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "The PH domain proteins IPIP27A and B link OCRL1 to receptor recycling in the endocytic pathway."
    Noakes C.J., Lee G., Lowe M.
    Mol. Biol. Cell 22:606-623(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FAM109A AND FAM109B.
  10. "Crystal structure of INPP5B in complex with phosphatidylinositol 4-phosphate (CASP target)."
    Structural genomics consortium (SGC)
    Submitted (JUL-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 339-646 IN COMPLEX WITH MAGNESIUM AND PHOSPHATIDYLINOSITOL 4-PHOSPHATE.

Entry informationi

Entry nameiI5P2_HUMAN
AccessioniPrimary (citable) accession number: P32019
Secondary accession number(s): C9J6U5
, Q5VSG9, Q5VSH0, Q5VSH1, Q658Q5, Q6P6D4, Q6PD53, Q86YE1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: December 15, 2009
Last modified: November 26, 2014
This is version 139 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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